1000 Structures solved at X06DA-PXIII
The macromolecular crystallography beamline X06DA-PXIII has reached 1,000 structures in the Protein Data Bank (PDB) on February 22, 2017.
The macromolecular crystallography beamline X06DA-PXIII has reached 1,000 structures in the Protein Data Bank (PDB) on February 22, 2017. This performance has been achieved in only 9 years user operation and counts for about 2/3 of the available beamtime, which is proposed to academic users. The other 1/3 is used by researchers from international pharmaceutical companies in a partnership in place since the start of the beamline.
Looking at the number of PDB depositions, the super bending magnet (BM) beamline X06DA-PXIII is currently the best performing BM worldwide and is amongst the top 15 most productive beamlines, a ranking dominated by insertion device sources. X06DA-PXIII does exhibit performance comparable to undulators and therefore provides a very high throughput. In addition, X06DA-PXIII offers hardware [1] and software tools that are highly suited for experimental phasing [2], in particular native SAD (single-wavelength anomalous dispersion). The current increase in structures solved by native SAD reflects the routine use of a simple and fast data collection protocol developed at X06DA-PXIII [3,4].
An integrated crystallization facility further complements the beamline capabilities and contributes to help structural biologists getting crystallographic structures in the most efficient manner [5].
We warmly congratulate our long term users - A. Mitschler/A. Podjarny, A. Mattevi/S. Pasqualato, T. Maier and A. Prota/M. Steinmetz - who have deposited the 1,000th structure at X06DA-PXIII.
Looking at the number of PDB depositions, the super bending magnet (BM) beamline X06DA-PXIII is currently the best performing BM worldwide and is amongst the top 15 most productive beamlines, a ranking dominated by insertion device sources. X06DA-PXIII does exhibit performance comparable to undulators and therefore provides a very high throughput. In addition, X06DA-PXIII offers hardware [1] and software tools that are highly suited for experimental phasing [2], in particular native SAD (single-wavelength anomalous dispersion). The current increase in structures solved by native SAD reflects the routine use of a simple and fast data collection protocol developed at X06DA-PXIII [3,4].
An integrated crystallization facility further complements the beamline capabilities and contributes to help structural biologists getting crystallographic structures in the most efficient manner [5].
We warmly congratulate our long term users - A. Mitschler/A. Podjarny, A. Mattevi/S. Pasqualato, T. Maier and A. Prota/M. Steinmetz - who have deposited the 1,000th structure at X06DA-PXIII.